Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation
Several motile processes are responsible for the movement of proteins into and within the flagellar membrane, but little is known about the process by which specific proteins (either actin-associated or not) are targeted to protozoan flagellar membranes. Actin is a major cytoskeleton protein, while...
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2009-01-01
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doaj-ef48226b42034e189188624959fc729f2020-11-25T00:43:36ZengSociedade Brasileira de GenéticaGenetics and Molecular Biology1415-47571678-46852009-01-0132365266510.1590/S1415-47572009000300033Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formationMichely C. DinizMarcília P. CostaAna C.L. PachecoMichel T. KamimuraSamara C. SilvaLaura D.G. CarneiroAna P.L. SousaCarlos E.A. SoaresCeleste S.F. SouzaDiana Magalhães de OliveiraSeveral motile processes are responsible for the movement of proteins into and within the flagellar membrane, but little is known about the process by which specific proteins (either actin-associated or not) are targeted to protozoan flagellar membranes. Actin is a major cytoskeleton protein, while polymerization and depolymerization of parasite actin and actin-interacting proteins (AIPs) during both processes of motility and host cell entry might be key events for successful infection. For a better understanding the eukaryotic flagellar dynamics, we have surveyed genomes, transcriptomes and proteomes of pathogenic Leishmania spp. to identify pertinent genes/proteins and to build in silico models to properly address their putative roles in trypanosomatid virulence. In a search for AIPs involved in flagellar activities, we applied computational biology and proteomic tools to infer from the biological meaning of coronins and Arp2/3, two important elements in phagosome formation after parasite phagocytosis by macrophages. Results presented here provide the first report of Leishmania coronin and Arp2/3 as flagellar proteins that also might be involved in phagosome formation through actin polymerization within the flagellar environment. This is an issue worthy of further in vitro examination that remains now as a direct, positive bioinformatics-derived inference to be presented.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572009000300033actin-interacting proteins (AIPs)flagellar proteinsLeishmaniacoronin and Arp2/3phagosome |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Michely C. Diniz Marcília P. Costa Ana C.L. Pacheco Michel T. Kamimura Samara C. Silva Laura D.G. Carneiro Ana P.L. Sousa Carlos E.A. Soares Celeste S.F. Souza Diana Magalhães de Oliveira |
spellingShingle |
Michely C. Diniz Marcília P. Costa Ana C.L. Pacheco Michel T. Kamimura Samara C. Silva Laura D.G. Carneiro Ana P.L. Sousa Carlos E.A. Soares Celeste S.F. Souza Diana Magalhães de Oliveira Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation Genetics and Molecular Biology actin-interacting proteins (AIPs) flagellar proteins Leishmania coronin and Arp2/3 phagosome |
author_facet |
Michely C. Diniz Marcília P. Costa Ana C.L. Pacheco Michel T. Kamimura Samara C. Silva Laura D.G. Carneiro Ana P.L. Sousa Carlos E.A. Soares Celeste S.F. Souza Diana Magalhães de Oliveira |
author_sort |
Michely C. Diniz |
title |
Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
title_short |
Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
title_full |
Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
title_fullStr |
Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
title_full_unstemmed |
Actin-interacting and flagellar proteins in Leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
title_sort |
actin-interacting and flagellar proteins in leishmania spp.: bioinformatics predictions to functional assignments in phagosome formation |
publisher |
Sociedade Brasileira de Genética |
series |
Genetics and Molecular Biology |
issn |
1415-4757 1678-4685 |
publishDate |
2009-01-01 |
description |
Several motile processes are responsible for the movement of proteins into and within the flagellar membrane, but little is known about the process by which specific proteins (either actin-associated or not) are targeted to protozoan flagellar membranes. Actin is a major cytoskeleton protein, while polymerization and depolymerization of parasite actin and actin-interacting proteins (AIPs) during both processes of motility and host cell entry might be key events for successful infection. For a better understanding the eukaryotic flagellar dynamics, we have surveyed genomes, transcriptomes and proteomes of pathogenic Leishmania spp. to identify pertinent genes/proteins and to build in silico models to properly address their putative roles in trypanosomatid virulence. In a search for AIPs involved in flagellar activities, we applied computational biology and proteomic tools to infer from the biological meaning of coronins and Arp2/3, two important elements in phagosome formation after parasite phagocytosis by macrophages. Results presented here provide the first report of Leishmania coronin and Arp2/3 as flagellar proteins that also might be involved in phagosome formation through actin polymerization within the flagellar environment. This is an issue worthy of further in vitro examination that remains now as a direct, positive bioinformatics-derived inference to be presented. |
topic |
actin-interacting proteins (AIPs) flagellar proteins Leishmania coronin and Arp2/3 phagosome |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572009000300033 |
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